The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin. / Chen, Shuai; Synowsky, Silvia; Tinti, Michele; MacKintosh, Carol.
In: Trends in Endocrinology and Metabolism, Vol. 22, No. 11, 11.2011, p. 429-436.Research output: Contribution to journal › Scientific review
}
TY - JOUR
T1 - The capture of phosphoproteins by 14-3-3 proteins mediates actions of insulin
A1 - Chen,Shuai
A1 - Synowsky,Silvia
A1 - Tinti,Michele
A1 - MacKintosh,Carol
AU - Chen,Shuai
AU - Synowsky,Silvia
AU - Tinti,Michele
AU - MacKintosh,Carol
PY - 2011/11
Y1 - 2011/11
N2 - <p>How does signalling via PI3K-PKB (AKT)-mTORC1-p70S6K and ERK-p90RSK mediate wide-ranging physiological responses to insulin? Quantitative proteomics and biochemical experiments are revealing that these signalling pathways induce the phosphorylation of large and overlapping sets of proteins, which are then captured by phosphoprotein-binding proteins named 14-3-3 s. The 14-3-3 s are dimers; that dock onto dual-phosphorylated sites in a configuration with special signalling and mechanical properties. They interact with the Rab GTPase-activating proteins AS160 and TBC1D1 to regulate glucose uptake into target tissues in response to insulin and energy stress. Dynamic patterns in the 14-3-3-binding phosphoproteome are providing new insights into how insulin triggers coherent shifts in metabolism that are integrated with other cellular response systems.</p>
AB - <p>How does signalling via PI3K-PKB (AKT)-mTORC1-p70S6K and ERK-p90RSK mediate wide-ranging physiological responses to insulin? Quantitative proteomics and biochemical experiments are revealing that these signalling pathways induce the phosphorylation of large and overlapping sets of proteins, which are then captured by phosphoprotein-binding proteins named 14-3-3 s. The 14-3-3 s are dimers; that dock onto dual-phosphorylated sites in a configuration with special signalling and mechanical properties. They interact with the Rab GTPase-activating proteins AS160 and TBC1D1 to regulate glucose uptake into target tissues in response to insulin and energy stress. Dynamic patterns in the 14-3-3-binding phosphoproteome are providing new insights into how insulin triggers coherent shifts in metabolism that are integrated with other cellular response systems.</p>
U2 - 10.1016/j.tem.2011.07.005
DO - 10.1016/j.tem.2011.07.005
M1 - Scientific review
JO - Trends in Endocrinology and Metabolism
JF - Trends in Endocrinology and Metabolism
SN - 1043-2760
IS - 11
VL - 22
SP - 429
EP - 436
ER -